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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Bacillus subtilis and UniProt Accession P94494

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.1 alanine racemase
IUBMB Comments
A pyridoxal-phosphate protein.
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Bacillus subtilis
UNIPROT: P94494
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Bacillus subtilis
Reaction Schemes
Synonyms
d-alanine racemase, alrbax, mbalr2, l-alanine racemase, ecalr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alanine racemase
287088, 287089
-
L-Alanine racemase
-
-
-
-
L-Alanine:D-alanine racemase
-
-
-
-
MurI
275559
-
Racemase, alanine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-alanine = D-alanine
show the reaction diagram
the active site of the alanine racemase reacts asymmetrically with the enantiomers of the substrate and has a conformation which greatly favors the D-enantiomer
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
SYSTEMATIC NAME
IUBMB Comments
alanine racemase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-06-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine
D-alanine
show the reaction diagram
-
-
-
r
L-Ala
D-Ala
show the reaction diagram
L-alanine
D-alanine
show the reaction diagram
additional information
?
-
-
exchange of the alpha-hydrogen of D-Ala and L-Ala with D2O
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-alanine
D-alanine
show the reaction diagram
P10725, P94494
-
-
-
r
L-alanine
D-alanine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-Chloro-D-alanine
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. Glutamate racemase (MurI) is a pyridoxal 5'-phosphate-independent racemase and is therefore unable to undergo the same mechanism of inhibition as Alr with BCDA
D-Chloroalanine
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Ki: 0.005 mM, competitive
L-chloroalanine
-
Ki: 1.71 mM, noncompetitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.9
L-alanine
pH 7.6, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1190
L-alanine
pH 7.6, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
201.7
L-alanine
pH 7.6, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
beta-Chloro-D-alanine
pH 7.6, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 10.5
yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
7.5
-
assay at
9.5
dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 11
pH 8.5: 42% of max. activity, pH 11: 58% of max. activity, yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
8.5 - 11
pH 8.5: 35% of max. activity, pH 11: 8% of max. activity, dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
50
dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
30°C: approx. 25% of max. activity, 70°C: approx. 8% of max. activity, yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
30 - 60
30°C and 60°C: approx. 20% of max. activity, dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43650
precided weight from primary sequence of 394 amino acids, yncD
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant expression in D-Alanine auxotrophic Escherichia coli strain MB2159 and DN1686, a D-Ala auxotrophic mutant
enzyme expression in Escherichia coli strain BL21(DE3)/pETALR
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gene alr, recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression in D-Alanine auxotrophic Escherichia coli strains MB2159 and DN1686, a D-Ala auxotrophic mutant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babu, U.M.; Johnston, R.B.
D2O-alanine exchange reactions catalyzed by alanine racemase and glutamic pyruvic transaminase
Biochem. Biophys. Res. Commun.
58
460-466
1974
Bacillus subtilis
Manually annotated by BRENDA team
Henderson, L.L.; Johnson, R.B.
Inhibition studies of the enantiomers of beta-chloroalanine on purified alanine racemase from Bacillus subtilis
Biochem. Biophys. Res. Commun.
68
793-798
1976
Bacillus subtilis
Manually annotated by BRENDA team
Tanizawa, K.; Ohshima, A.; Scheidegger, A.; Inagaki, K.; Tanaka, H.; Soda, K.
Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure prediction
Biochemistry
27
1311-1316
1988
Bacillus subtilis, Geobacillus stearothermophilus, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Yoshimura, T.; Esaki, N.; Soda, K.
Structure and function of alanine racemase
Bull. Inst. Chem. Res. Kyoto Univ.
70
378-384
1992
Bacillus subtilis, Enterococcus faecalis, Geobacillus stearothermophilus, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team
Yoshimura, T.; Goto, M.
D-amino acids in the brain: structure and function of pyridoxal phosphate-dependent amino acid racemases
FEBS J.
275
3527-3537
2008
Bacillus subtilis, Bipolaris zeicola, Escherichia coli, Geobacillus stearothermophilus (P10724), Salmonella enterica subsp. enterica serovar Typhimurium, Tolypocladium inflatum
Manually annotated by BRENDA team
Pierce, K.J.; Salifu, S.P.; Tangney, M.
Gene cloning and characterization of a second alanine racemase from Bacillus subtilis encoded by yncD
FEMS Microbiol. Lett.
283
69-74
2009
Bacillus subtilis 168 (P10725), Bacillus subtilis 168 (P94494), Bacillus subtilis, Bacillus subtilis (P10725), Bacillus subtilis (P94494), no activity in Bacillus subtilis, no activity in Bacillus subtilis DN1686
Manually annotated by BRENDA team
Zhu, L.; Tao, R.; Wang, Y.; Jiang, Y.; Lin, X.; Yang, Y.; Zheng, H.; Jiang, W.; Yang, S.
Removal of L-alanine from the production of L-2-aminobutyric acid by introduction of alanine racemase and D-amino acid oxidase
Appl. Microbiol. Biotechnol.
90
903-910
2011
Bacillus subtilis
Manually annotated by BRENDA team
Prosser, G.A.; Rodenburg, A.; Khoury, H.; de Chiara, C.; Howell, S.; Snijders, A.P.; de Carvalho, L.P.
Glutamate racemase is the primary target of beta-chloro-D-alanine in Mycobacterium tuberculosis
Antimicrob. Agents Chemother.
60
6091-6099
2016
Bacillus subtilis 168 (P94556), Bacillus subtilis (P94556), Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WPW9), Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WPW9)
Manually annotated by BRENDA team
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